Dresden 2026 – scientific programme

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BP: Fachverband Biologische Physik

BP 39: Focus Session: Theoretical Modeling and Simulation of Biomolecular Condensates III (joint session CPP/BP)

BP 39.2: Talk

Friday, March 13, 2026, 10:00–10:15, ZEU/0260

Born to Condense: Polysomes Drive Co-Translational Condensation of Biomolecular Condensate Proteins — •Zhouyi He, Jens-Uwe Sommer, and Tyler Harmon — Leibniz Institute of Polymer Research, 01069, Dresden, Germany

Biomolecular condensates formed by protein LLPS are ubiquitous and crucial in cells. While the physics and functions of LLPS are well studied, its interplay with protein synthesis, translation, remains largely unexplored. Here we propose Co-Translational Condensation (CTC), a mechanism in which nascent protein chains of polysomes, multiple ribosomes on one mRNA, interact with condensates, localizing translation to condensate surfaces. Using coarse-grained simulations, we show that protein domain architecture dictates the extend of CTC, consistent with a Langmuir adsorption model. Bioinformatic analysis reveals that most condensate-associated proteins have architectures favoring CTC, with strong interaction regions of nascent chains exposed on polysomes. Dynamically, simulation and reaction-diffusion modeling reveal that CTC is kinetically feasible within typical polysome lifetimes, either through large polysomes nucleating new condensates or via diffusion to pre-existing condensates. As a case study, we demonstrate that CTC enhances post-translational modifications by minimizing unmodified intermediates. More broadly, we anticipate CTC may also influence protein folding, misfolding, and signal-integration latency. Together, our results establish CTC as a general mechanism coupling translation with phase separation, with broad implications for protein evolution, cellular organization, and synthetic biology.

Keywords: Biomolecular condensates; Phase separation; Polysome; Translation; Condensation